Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

An antibody class with a common CDRH3 motif broadly neutralizes sarbecoviruses
Lihong Liu, Sho Iketani, Yicheng Guo, et al.
Science Translational Medicine (2022) Vol. 14, Iss. 646
Open Access | Times Cited: 47

Showing 1-25 of 47 citing articles:

Alarming antibody evasion properties of rising SARS-CoV-2 BQ and XBB subvariants
Qian Wang, Sho Iketani, Zhiteng Li, et al.
Cell (2022) Vol. 186, Iss. 2, pp. 279-286.e8
Open Access | Times Cited: 743
Antibody evasion by SARS-CoV-2 Omicron subvariants BA.2.12.1, BA.4 and BA.5
Qian Wang, Yicheng Guo, Sho Iketani, et al.
Nature (2022) Vol. 608, Iss. 7923, pp. 603-608
Open Access | Times Cited: 705
Antigenicity and receptor affinity of SARS-CoV-2 BA.2.86 spike
Qian Wang, Yicheng Guo, Liyuan Liu, et al.
Nature (2023) Vol. 624, Iss. 7992, pp. 639-644
Open Access | Times Cited: 150
Antigenic characterization of the SARS-CoV-2 Omicron subvariant BA.2.75
Qian Wang, Sho Iketani, Zhiteng Li, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 11, pp. 1512-1517.e4
Open Access | Times Cited: 98
COVID-19 drug discovery and treatment options
Jasper Fuk‐Woo Chan, Shuofeng Yuan, Hin Chu, et al.
Nature Reviews Microbiology (2024) Vol. 22, Iss. 7, pp. 391-407
Closed Access | Times Cited: 17
Targeted isolation of diverse human protective broadly neutralizing antibodies against SARS-like viruses
Wanting He, Rami Musharrafieh, Ge Song, et al.
Nature Immunology (2022) Vol. 23, Iss. 6, pp. 960-970
Open Access | Times Cited: 56
Protective neutralizing epitopes in SARS‐CoV‐2
Hejun Liu, Ian A. Wilson
Immunological Reviews (2022) Vol. 310, Iss. 1, pp. 76-92
Open Access | Times Cited: 39
Structural basis for a conserved neutralization epitope on the receptor-binding domain of SARS-CoV-2
Kuan-Ying A. Huang, Xiaorui Chen, Arpita Mohapatra, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 35
Antibody evasion by SARS-CoV-2 Omicron subvariants BA.2.12.1, BA.4, and BA.5
Qian Wang, Yicheng Guo, Sho Iketani, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 32
Alarming antibody evasion properties of rising SARS-CoV-2 BQ and XBB subvariants
Qian Wang, Sho Iketani, Zhiteng Li, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 29
Broadly neutralizing antibodies against COVID-19
Daming Zhou, Jingshan Ren, Elizabeth E. Fry, et al.
Current Opinion in Virology (2023) Vol. 61, pp. 101332-101332
Open Access | Times Cited: 19
Evolving antibody evasion and receptor affinity of the Omicron BA.2.75 sublineage of SARS-CoV-2
Qian Wang, Zhiteng Li, Yicheng Guo, et al.
iScience (2023) Vol. 26, Iss. 11, pp. 108254-108254
Open Access | Times Cited: 19
Antibodies targeting a quaternary site on SARS-CoV-2 spike glycoprotein prevent viral receptor engagement by conformational locking
Lihong Liu, Ryan G. Casner, Yicheng Guo, et al.
Immunity (2023) Vol. 56, Iss. 10, pp. 2442-2455.e8
Open Access | Times Cited: 16
Comprehensive Overview of Broadly Neutralizing Antibodies against SARS-COV-2 Variants
Lingyan Cui, Tingting Li, Wenhui Xue, et al.
(2024)
Open Access | Times Cited: 6
Recurrent SARS-CoV-2 spike mutations confer growth advantages to select JN.1 sublineages
Qian Wang, Ian A. Mellis, Anthony Bowen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 5
Design of SARS-CoV-2 RBD Immunogens to Focus Immune Responses Towards Conserved Coronavirus Epitopes
Caitlin Harris, A. Brenda Kapingidza, James Emmanuel San, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Closed Access
Comprehensive Overview of Broadly Neutralizing Antibodies against SARS-CoV-2 Variants
Lingyan Cui, Tingting Li, Wenhui Xue, et al.
Viruses (2024) Vol. 16, Iss. 6, pp. 900-900
Open Access | Times Cited: 4
Antigenic characterization of the SARS-CoV-2 Omicron subvariant BA.2.75
Qian Wang, Sho Iketani, Zhiteng Li, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 18
Antibodies that neutralize all current SARS-CoV-2 variants of concern by conformational locking
Lihong Liu, Ryan G. Casner, Yicheng Guo, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 11
The D Gene in CDR H3 Determines a Public Class of Human Antibodies to SARS-CoV-2
Meng Yuan, Ian A. Wilson
Vaccines (2024) Vol. 12, Iss. 5, pp. 467-467
Open Access | Times Cited: 3
Broad cross neutralizing antibodies against sarbecoviruses generated by SARS-CoV-2 infection and vaccination in humans
Yabin Hu, Qian Wu, Fangfang Chang, et al.
npj Vaccines (2024) Vol. 9, Iss. 1
Open Access | Times Cited: 3
Broadly neutralizing antibodies targeting a conserved silent face of spike RBD resist extreme SARS-CoV-2 antigenic drift
Ge Song, Meng Yuan, Hejun Liu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 9
SARS-CoV-2 antibodies recognize 23 distinct epitopic sites on the receptor binding domain
Jiansheng Jiang, Christopher T. Boughter, Javeed Ahmad, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 9
Antigenicity and receptor affinity of SARS-CoV-2 BA.2.86 spike
Qian Wang, Yicheng Guo, Liyuan Liu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 9
Human antibodies to SARS-CoV-2 with a recurring YYDRxG motif retain binding and neutralization to variants of concern including Omicron
Hejun Liu, Chengzi I. Kaku, Ge Song, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 15
Page 1 - Next Page

Scroll to top